Reviewed, UniProtKB/Swiss-Prot Q6FKS5 (HAT1_CANGA)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase type B catalytic subunit
    EC=2.3.1.48

Gene names

Name:	HAT1
Ordered Locus Names:	CAGL0L09042g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair By similarity.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the HAT1 family. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro histone acetylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell histone acetyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	Histone acetyltransferase type B catalytic subunit		PRO_0000227720
Regions
	Domain	142 – 306	165	N-acetyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q6FKS5-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 7D26B0E7E97840D4	FASTA	388	45,819
	10 20 30 40 50 60 MSIDDFKPEK WTISSNEALK LSLVSEDNAI QFSPTFTYPI FGTEEQIFGY KDLVIHLAFD 70 80 90 100 110 120 AITFKPFLNV KFSSKFEGSE EELVNIKEKL LEYLPIDDTI YKDEEKWIDS FKKEQESIEA 130 140 150 160 170 180 YKNDQNIDEY KIDNADFEIY KVNLQDPKMK RFHRRIQIFS LLFIEAASYI DEDDPKWEIF 190 200 210 220 230 240 IVQTKKDKKF VGYATAYNYW YYPGANNFDS ESKYRYRGKI SQFLILPPYQ GRGHGSHLYN 250 260 270 280 290 300 SIVKNWRNDS SILEIVVEDP NESFDDLRDV NDLEMLYKDG FFNKLPQERP IPNAWIESTR 310 320 330 340 350 360 LKYKIEKRQF SRLLEMILLS TGSNNFEYQV KQRLLIKNKD GLEGMEVSDI KDALNKSFES 370 380 LREDYDRILG KCQFSNDADG PSKKKIKT

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380958 Genomic DNA. Translation: CAG62139.1.
RefSeq	XP_449169.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FKS5.
Genome annotation databases
GeneID	2891100.
GenomeReviews	Gene locus CAGL0L09042g in contig CR380958_GR.
KEGG	cgr:CAGL0L09042g.
Phylogenomic databases
HOGENOM	Q6FKS5.
OMA	FESHISA.
Enzyme and pathway databases
BRENDA	2.3.1.48. 189220.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GCN5-rel_AcTrfase. IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. IPR013523. Hist_AcTrfase_HAT1_C. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:1.10.10.390. Histone_AcTrfase_HAT1_C. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HAT1_CANGA

Accession

Primary (citable) accession number: Q6FKS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)